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Protein

Beta-enolase

Gene

Eno3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Appears to have a function in striated muscle development and regeneration.

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm10358), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Beta-enolase (Eno3), Alpha-enolase (Eno1), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245MagnesiumBy similarity1
Metal bindingi293MagnesiumBy similarity1
Binding sitei293SubstrateBy similarity1
Metal bindingi318MagnesiumBy similarity1
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aging Source: Ensembl
  • glycolytic process Source: CAFA
  • response to drug Source: Ensembl
  • skeletal muscle tissue regeneration Source: Ensembl

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11 3474
ReactomeiR-MMU-70171 Glycolysis
R-MMU-70263 Gluconeogenesis
UniPathwayiUPA00109; UER00187

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name:
MSE
Skeletal muscle enolase
Gene namesi
Name:Eno3
Synonyms:Eno-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95395 Eno3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001341082 – 434Beta-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei26PhosphothreonineBy similarity1
Modified residuei44PhosphotyrosineBy similarity1
Modified residuei72PhosphothreonineBy similarity1
Modified residuei83PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei176PhosphoserineBy similarity1
Modified residuei205PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei236PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP21550
PaxDbiP21550
PeptideAtlasiP21550
PRIDEiP21550

2D gel databases

SWISS-2DPAGEP21550
UCD-2DPAGEP21550

PTM databases

iPTMnetiP21550
PhosphoSitePlusiP21550

Expressioni

Tissue specificityi

Brain (at protein level). The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I.2 Publications

Developmental stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube.2 Publications

Inductioni

Levels decrease in degenerating myofibers, and increase with their regeneration.

Gene expression databases

BgeeiENSMUSG00000060600
CleanExiMM_ENO3
ExpressionAtlasiP21550 baseline and differential
GenevisibleiP21550 MM

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199453, 4 interactors
IntActiP21550, 4 interactors
MINTiP21550
STRINGi10090.ENSMUSP00000072620

Structurei

3D structure databases

ProteinModelPortaliP21550
SMRiP21550
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670 Eukaryota
COG0148 LUCA
GeneTreeiENSGT00910000144064
HOGENOMiHOG000072174
HOVERGENiHBG000067
InParanoidiP21550
KOiK01689
OMAiQEFLVVP
OrthoDBiEOG091G07NH
PhylomeDBiP21550
TreeFamiTF300391

Family and domain databases

CDDicd03313 enolase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SFLDiSFLDG00178 enolase, 1 hit
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKARYLGK GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLVLPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE
260 270 280 290 300
FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD
310 320 330 340 350
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEALGDK AVFAGRKFRN PKAK
Length:434
Mass (Da):47,025
Last modified:January 23, 2007 - v3
Checksum:iA1F757D83709D2B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti234 – 235AG → NA in AAA37554 (PubMed:2734297).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61600 Genomic DNA Translation: CAA43797.1
X57747 mRNA Translation: CAA40913.1
X62667 mRNA Translation: CAA44540.1
AK002485 mRNA Translation: BAB22137.1
BC013460 mRNA Translation: AAH13460.1
M20745 mRNA Translation: AAA37554.1
CCDSiCCDS24961.1
PIRiS17109 NOMSB
RefSeqiNP_001129534.1, NM_001136062.2
NP_001263214.1, NM_001276285.1
NP_031959.1, NM_007933.3
XP_006532225.1, XM_006532162.3
UniGeneiMm.251322
Mm.491763

Genome annotation databases

EnsembliENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600
ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600
ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600
GeneIDi13808
KEGGimmu:13808
UCSCiuc007jvx.3 mouse

Similar proteinsi

Entry informationi

Entry nameiENOB_MOUSE
AccessioniPrimary (citable) accession number: P21550
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 177 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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